Lysine Acetylation Regulates Alanyl-tRNA Synthetase Activity in Escherichia coli.
Lysine Acetylation Regulates Alanyl-tRNA Synthetase Activity in Escherichia coli.
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DOI：
10.3390/genes9100473
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发表时间：
2018-09-28
期刊：
影响因子：
3.5
通讯作者：
Tamura K
中科院分区：
文献类型：
--
作者：
Umehara T;Kosono S;Söll D;Tamura K
蛋白质赖氨酸乙酰化是一个广泛保守的翻译后修饰在所有三个领域的生命。赖氨酸乙酰化经常发生在许多生物体的氨基酰基- trna合成酶（aars）中。在本研究中，我们确定了大肠杆菌II类丙烯酰trna合成酶（AlaRS）中赖氨酸-73 （K73）天然乙酰化对其丙烯酰化活性的影响。我们利用扩展的遗传密码系统在大肠杆菌中制备了一株在73位加入了nε -乙酰赖氨酸的AlaRS K73Ac变异株。与野生型（WT）相比，AlaRS K73Ac变异表现出较低的活性。在大肠杆菌中，烟酰胺处理或cobb -缺失导致AlaRS K73Ac乙酰化水平升高，并强烈降低丙烯酰化活性。我们假设AlaRS的丙烯酰化受到K73乙酰化的影响，并且这种修饰在体内对CobB去乙酰化酶敏感。我们还发现大肠杆菌在体内表达两种CobB亚型（CobB- l和CobB- s）。CobB-S在体外显示了AlaRS K73Ac变体的去乙酰化酶活性。我们的结果表明赖氨酸乙酰化在控制aars活性和蛋白质合成方面具有潜在的调节作用。
Protein lysine acetylation is a widely conserved posttranslational modification in all three domains of life. Lysine acetylation frequently occurs in aminoacyl-tRNA synthetases (aaRSs) from many organisms. In this study, we determined the impact of the naturally occurring acetylation at lysine-73 (K73) in Escherichia coli class II alanyl-tRNA synthetase (AlaRS) on its alanylation activity. We prepared an AlaRS K73Ac variant in which Nε-acetyl-l-lysine was incorporated at position 73 using an expanded genetic code system in E. coli. The AlaRS K73Ac variant showed low activity compared to the AlaRS wild type (WT). Nicotinamide treatment or CobB-deletion in an E. coli led to elevated acetylation levels of AlaRS K73Ac and strongly reduced alanylation activities. We assumed that alanylation by AlaRS is affected by K73 acetylation, and the modification is sensitive to CobB deacetylase in vivo. We also showed that E. coli expresses two CobB isoforms (CobB-L and CobB-S) in vivo. CobB-S displayed the deacetylase activity of the AlaRS K73Ac variant in vitro. Our results imply a potential regulatory role for lysine acetylation in controlling the activity of aaRSs and protein synthesis.
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